EC Number |
---|
2.5.1.47 | - |
2.5.1.47 | analysis of the three-dimensional crystal structure of O-acetyl-L-serine sulfhydrylase enzyme complexed with cysteine and pyridoxal 5'-phosphate ligands, PDB ID 3BM5, determined by X-ray crystallography |
2.5.1.47 | complex with inhibitory pentapeptides MNYDI (10 mM HEPES, pH 8.0, 25 mM NaCl, 8.8 mM peptide), MNKGI (20 mM HEPES, pH 7.5, 20 mM NaCl, 12.5 mM peptide), MNWNI (10 mM HEPES, pH 7.5, 25 mM NaCl, 7.5 mM peptide), MNYFI (20 mM HEPES, pH 8.0, 20 mM NaCl, 12.7 mM peptide), MNENI (10 mM HEPES, pH 7.5, 25 mM NaCl, 9.4 mM peptide), and MNETI (20 mM HEPES, pH 7.5, 20 mM NaCl, 9.4 mM peptide), reservoir solution is 100 mM HEPES, pH 7.5, between 1.8 and 2.1 M (NH4)2SO4, and polyethylene glycol 400, except for the complex with MNWNI (100 mM CAPS, pH 10.5, 1.75 (NH4)2SO4, and 0.2 M Li2SO4), the cryoprotection solution contains glycerol, hanging drop vapor diffusion method, diffraction data are measured at -183°C |
2.5.1.47 | construction of a model of the cysteine synthase complex composed of the enzymes serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL. Binding energy calculations suggest that, consistent with experiments, a ratio of two OAS-TL dimers to one SAT hexamer is likely |
2.5.1.47 | crystal structure of the enzyme with chloride bound at an allosteric site and sulfate bound at the active site |
2.5.1.47 | hanging drop vapor diffusion method, using 100 mM sodium citrate, pH 5.6, 100 mM ammonium sulfate, 20% (w/v) PEG 4000 |
2.5.1.47 | hanging-drop vapor diffusion method, structure of O-acetylserine sulfhydrylase B solved to 2.3 A |
2.5.1.47 | hanging-drop vapour-diffusion method, crystals belong to the tetragonal space group P4(1), with unit cell parameters a = 80.3, b = 80.3, c = 112.2 A, two molecules per asymmetric unit and a complete data set is collected to a resolution of 1.86 A |
2.5.1.47 | homology modeling of structure |
2.5.1.47 | identification of inhibitors by docking into crystal structure, PDB entry 2Q3C |